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Science 12 April 1996:
Vol. 272. no. 5259, pp. 268 - 270
DOI: 10.1126/science.272.5259.268
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Reports

Accurate Processing of a Eukaryotic Precursor Ribosomal RNA by Ribonuclease MRP in Vitro

Zoi Lygerou, Christine Allmang, David Tollervey, Bertrand Séraphin *

Very few of the enzymes required for eukaryotic precursor ribosomal RNA (pre-rRNA) processing have been identified. Ribonuclease (RNase) MRP was characterized as a nuclease that cleaves mitochondrial replication primers, but it is predominantly nucleolar. Previous genetic evidence revealed that this ribonucleoprotein is required, directly or indirectly, for cleavage of the yeast pre-rRNA in vivo at site A3. Here, an in vitro processing system that accurately reproduces this cleavage is described. Biochemical purification and the use of extracts depleted of the MRP RNA demonstrate that endonucleolytic cleavage of the pre-rRNA is directly mediated by RNase MRP. This establishes a role for RNase MRP in the nucleolus.

European Molecular Biology Laboratory, Meyerhofstrasse 1, D-69117 Heidelberg, Germany.
* To whom correspondence should be addressed.


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Deletion of the Three Distal S1 Motifs of Saccharomyces cerevisiae Rrp5p Abolishes Pre-rRNA Processing at Site A2 without Reducing the Production of Functional 40S Subunits.
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The RNA catabolic enzymes Rex4p, Rnt1p, and Dbr1p show genetic interaction with trans-acting factors involved in processing of ITS1 in Saccharomyces cerevisiae pre-rRNA.
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T. Gill, T. Cai, J. Aulds, S. Wierzbicki, and M. E. Schmitt (2004)
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Purification, Cloning, and Characterization of XendoU, a Novel Endoribonuclease Involved in Processing of Intron-encoded Small Nucleolar RNAs in Xenopus laevis.
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Cold Spring Harb Symp Quant Biol 66, 575-590
   Abstract »    PDF »
Human H/ACA Small Nucleolar RNPs and Telomerase Share Evolutionarily Conserved Proteins NHP2 and NOP10.
V. Pogacic, F. Dragon, and W. Filipowicz (2000)
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Bop1 Is a Mouse WD40 Repeat Nucleolar Protein Involved in 28S and 5.8S rRNA Processing and 60S Ribosome Biogenesis.
Z. Strezoska, D. G. Pestov, and L. F. Lau (2000)
Mol. Cell. Biol. 20, 5516-5528
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In Vitro Assembly of Human H/ACA Small Nucleolar RNPs Reveals Unique Features of U17 and Telomerase RNAs.
F. Dragon and W. Filipowicz (2000)
Mol. Cell. Biol. 20, 3037-3048
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The Ribosomal RNA Processing Machinery Is Recruited to the Nucleolar Domain before RNA Polymerase I during Xenopus laevis Development.
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Protein trans-Acting Factors Involved in Ribosome Biogenesis in Saccharomyces cerevisiae.
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The nucleolar antigen Nop52, the human homologue of the yeast ribosomal RNA processing RRP1, is recruited at late stages of nucleologenesis.
T. Savino, R Bastos, E Jansen, and D Hernandez-Verdun (1999)
J. Cell Sci. 112, 1889-1900
   Abstract »    PDF »
Initiation of Mitochondrial DNA Replication by Transcription and R-loop Processing.
D. Y. Lee and D. A. Clayton (1998)
J. Biol. Chem. 273, 30614-30621
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Partially Processed pre-rRNA Is Preserved in Association with Processing Components in Nucleolus-derived Foci during Mitosis.
M. Dundr and M. O.J. Olson (1998)
Mol. Biol. Cell 9, 2407-2422
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Rpp2, an essential protein subunit of nuclear RNase P, is required for processing of precursor tRNAs and 35S precursor rRNA in Saccharomyces cerevisiae.
V. Stolc, A. Katz, and S. Altman (1998)
PNAS 95, 6716-6721
   Abstract »    Full Text »    PDF »
Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP.
J. R. Chamberlain, Y. Lee, W. S. Lane, and D. R. Engelke (1998)
Genes & Dev. 12, 1678-1690
   Abstract »    Full Text »
Processing of the Precursors to Small Nucleolar RNAs and rRNAs Requires Common Components.
E. Petfalski, T. Dandekar, Y. Henry, and D. Tollervey (1998)
Mol. Cell. Biol. 18, 1181-1189
   Abstract »    Full Text »
cDNA Cloning and Characterization of the Human U3 Small Nucleolar Ribonucleoprotein Complex-Associated 55-Kilodalton Protein.
H. Pluk, J. Soffner, R. Lührmann, and W. J. v. Venrooij (1998)
Mol. Cell. Biol. 18, 488-498
   Abstract »    Full Text »
Rpp1, an essential protein subunit of nuclear RNase P required for processing of precursor tRNA and 35S precursor rRNA in Saccharomyces cerevisiae.
V. Stolc and S. Altman (1997)
Genes & Dev. 11, 2926-2937
   Abstract »    Full Text »    PDF »
Rpp1, an essential protein subunit of nuclear RNase P required for processing of precursor tRNA and 35S precursor rRNA in Saccharomyces cerevisiae.
V. Stolc and S. Altman (1997)
Genes & Dev. 11, 2414-2425
   Abstract »    Full Text »    PDF »
Formation of 2',3'-Cyclic Phosphates at the 3' End of Human U6 Small Nuclear RNA in Vitro. IDENTIFICATION OF 2',3'-CYCLIC PHOSPHATES AT THE 3' ENDS OF HUMAN SIGNAL RECOGNITION PARTICLE AND MITOCHONDRIAL RNA PROCESSING RNAs.
J. Gu, G. Shumyatsky, N. Makan, and R. Reddy (1997)
J. Biol. Chem. 272, 21989-21993
   Abstract »    Full Text »    PDF »
Reconstitution of Functional Eukaryotic Ribosomes from Dictyostelium discoideum Ribosomal Proteins and RNA.
G. Mangiarotti and S. Chiaberge (1997)
J. Biol. Chem. 272, 19682-19687
   Abstract »    Full Text »    PDF »
Synthesis of functional eukaryotic ribosomal RNAs in trans: Development of a novel in vivo rDNA system for dissecting ribosome biogenesis.
W.-Q. Liang and M. J. Fournier (1997)
PNAS 94, 2864-2868
   Abstract »    Full Text »    PDF »
The family of box ACA small nucleolar RNAs is defined by an evolutionarily conserved secondary structure and ubiquitous sequence elements essential for RNA accumulation..
P Ganot, M Caizergues-Ferrer, and T Kiss (1997)
Genes & Dev. 11, 941-956
   Abstract »    PDF »
RNase mitochondrial RNA processing correctly cleaves a novel R loop at the mitochondrial DNA leading-strand origin of replication..
D Y Lee and D A Clayton (1997)
Genes & Dev. 11, 582-592
   Abstract »    PDF »
Characterization of two scleroderma autoimmune antigens that copurify with human ribonuclease P.
P. S. Eder, R. Kekuda, V. Stolc, and S. Altman (1997)
PNAS 94, 1101-1106
   Abstract »    Full Text »    PDF »
hPop5, a Protein Subunit of the Human RNase MRP and RNase P Endoribonucleases.
H. van Eenennaam, D. Lugtenberg, J. H. P. Vogelzangs, W. J. van Venrooij, and G. J. M. Pruijn (2001)
J. Biol. Chem. 276, 31635-31641
   Abstract »    Full Text »    PDF »


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